1ehk
From Proteopedia
(New page: 200px<br /><applet load="1ehk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ehk, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ehk.gif|left|200px]]<br /><applet load="1ehk" size=" | + | [[Image:1ehk.gif|left|200px]]<br /><applet load="1ehk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ehk, resolution 2.40Å" /> | caption="1ehk, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS'''<br /> | '''CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome c oxidase is a respiratory enzyme catalysing the | + | Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 A resolution using multiple anomalous dispersion (MAD) phasing and led to the discovery of a novel subunit IIa. A structure-based sequence alignment of this phylogenetically very distant oxidase with the other structurally known cytochrome oxidases leads to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases, e.g. a new electron transfer pathway leading directly from Cu(A) to Cu(B). Specific features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (O(2-), OH(-) or H(2)O) as bridging ligand at the active site and the mainly hydrophobic character of the interactions that stabilize the electron transfer complex between this oxidase and its substrate cytochrome c. New aspects of the proton pumping mechanism could be identified. |
==About this Structure== | ==About this Structure== | ||
| - | 1EHK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with BNG, CU, HEM, HAS and CUA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] Full crystallographic information is available from [http:// | + | 1EHK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=BNG:'>BNG</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=HAS:'>HAS</scene> and <scene name='pdbligand=CUA:'>CUA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| - | [[Category: Bartunik, H | + | [[Category: Bartunik, H D.]] |
| - | [[Category: Bourenkov, G | + | [[Category: Bourenkov, G P.]] |
[[Category: Buse, G.]] | [[Category: Buse, G.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Soulimane, T.]] | [[Category: Soulimane, T.]] | ||
| - | [[Category: Than, M | + | [[Category: Than, M E.]] |
[[Category: BNG]] | [[Category: BNG]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: thermus thermophilus]] | [[Category: thermus thermophilus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:49 2008'' |
Revision as of 10:27, 21 February 2008
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CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS
Overview
Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 A resolution using multiple anomalous dispersion (MAD) phasing and led to the discovery of a novel subunit IIa. A structure-based sequence alignment of this phylogenetically very distant oxidase with the other structurally known cytochrome oxidases leads to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases, e.g. a new electron transfer pathway leading directly from Cu(A) to Cu(B). Specific features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (O(2-), OH(-) or H(2)O) as bridging ligand at the active site and the mainly hydrophobic character of the interactions that stabilize the electron transfer complex between this oxidase and its substrate cytochrome c. New aspects of the proton pumping mechanism could be identified.
About this Structure
1EHK is a Protein complex structure of sequences from Thermus thermophilus with , , , and as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus., Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME, EMBO J. 2000 Apr 17;19(8):1766-76. PMID:10775261
Page seeded by OCA on Thu Feb 21 12:27:49 2008
Categories: Cytochrome-c oxidase | Protein complex | Thermus thermophilus | Bartunik, H D. | Bourenkov, G P. | Buse, G. | Huber, R. | Soulimane, T. | Than, M E. | BNG | CU | CUA | HAS | HEM | Membrane protein
